10.5452/MA-Q6982
Penteado, Renato Ferras; Iulek, Jorge
Herbaspirillum seropedicae Recombinase A, active form, wild type
modelarchive.org
2019
3D macromolecular model
2019-04-01
en
In this work we have performed in vitro, in vivo and in silico studies of Recombinase A from Herbaspirillum seropedicae (HsRecA) - Uniprot AC Q9F672 -, both the wild type and the L53Q mutant. This mutation is located at the Make ATP Work motif (MAW) and impairs the ATPase and DNA-strand exchange activities, however, it does not affect the binding of ADP, ATP and ssDNA.
At complementation studies of E. coli recA1 with the HsRecA L53Q mutant, changes in its phenotype under either MMS or UV challenge were not observed. Molecular dynamics simulations showed the L53Q point mutation did not cause large conformational changes in the HsRecA structure. However, there is a difference on dynamical cross-correlation movements of the residues involved in contacts within the ATP binding site and regions that hold the DNA binding sites. Additionally, a new hydrogen bond, formed between Q53 and T49, was hypothesized to allow an independent motion of the MAW motif from the hydrophobic core, what could explain the observed loss of activity of HsRecA L53Q.